Crystallization and preliminary X-ray studies of sialidase L from the leech Macrobdella decora

1998 ◽  
Vol 54 (1) ◽  
pp. 111-113 ◽  
Author(s):  
Yu Luo ◽  
Min-yuan Chou ◽  
Su-chen Li ◽  
Yu-teh Li ◽  
Ming Luo
Keyword(s):  
Escherichia Coli ◽  
Unit Cell ◽  
Data Sets ◽  
Molecular Replacement ◽  
Unit Cell Parameters ◽  
Solvent Content ◽  
X Ray ◽  
Cell Parameters ◽  
Mercury Derivative ◽  
Macrobdella Decora

Functional monomeric 83 kDa sialidase L, a NeuAcα2→3Gal-specific sialidase from Macrobdella leech, was expressed in Escherichia coli and readily crystallized by a macroseeding technique. The crystal belongs to space group P1 with unit-cell parameters a = 46.4, b = 69.3, c = 72.5 Å, α = 113.5, β = 95.4 and γ = 107.3°. There is one molecule per unit cell, giving a Vm = 2.4 Å3 Da−1 and a solvent content of 40%. Native and mercury-derivative data sets were collected to 2.0 Å resolution. Threading and molecular-replacement calculations confirmed the existence of a bacterial sialidase-like domain.

scholarly journals Crystallization and X-ray diffraction analysis of native and selenomethionine-substituted PhyH-DI fromBacillussp. HJB17

2017 ◽  
Vol 73 (11) ◽  
pp. 607-611
Author(s):  
Fang Lu ◽  
Bei Zhang ◽  
Yong Liu ◽  
Ying Song ◽  
Gangxing Guo ◽  
...  
Keyword(s):  
Unit Cell ◽  
Diffusion Method ◽  
Data Sets ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Solvent Content ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

Phytases are phosphatases that hydrolyze phytates to less phosphorylatedmyo-inositol derivatives and inorganic phosphate. β-Propeller phytases, which are very diverse phytases with improved thermostability that are active at neutral and alkaline pH and have absolute substrate specificity, are ideal substitutes for other commercial phytases. PhyH-DI, a β-propeller phytase fromBacillussp. HJB17, was found to act synergistically with other single-domain phytases and can increase their efficiency in the hydrolysis of phytate. Crystals of native and selenomethionine-substituted PhyH-DI were obtained using the vapour-diffusion method in a condition consisting of 0.2 Msodium chloride, 0.1 MTris pH 8.5, 25%(w/v) PEG 3350 at 289 K. X-ray diffraction data were collected to 3.00 and 2.70 Å resolution, respectively, at 100 K. Native PhyH-DI crystals belonged to space groupC121, with unit-cell parametersa = 156.84,b = 45.54,c = 97.64 Å, α = 90.00, β = 125.86, γ = 90.00°. The asymmetric unit contained two molecules of PhyH-DI, with a corresponding Matthews coefficient of 2.17 Å3 Da−1and a solvent content of 43.26%. Crystals of selenomethionine-substituted PhyH-DI belonged to space groupC2221, with unit-cell parametersa = 94.71,b= 97.03,c= 69.16 Å, α = β = γ = 90.00°. The asymmetric unit contained one molecule of the protein, with a corresponding Matthews coefficient of 2.44 Å3 Da−1and a solvent content of 49.64%. Initial phases for PhyH-DI were obtained from SeMet SAD data sets. These data will be useful for further studies of the structure–function relationship of PhyH-DI.

scholarly journals Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization

2012 ◽  
Vol 68 (7) ◽  
pp. 816-819 ◽  
Author(s):  
Benjamin Stieglitz ◽  
Katrin Rittinger ◽  
Lesley F. Haire
Keyword(s):  
Escherichia Coli ◽  
Protein Concentration ◽  
Unit Cell ◽  
Data Sets ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
One Step

An N-terminal fragment of human SHARPIN was recombinantly expressed inEscherichia coli, purified and crystallized. Crystals suitable for X-ray diffraction were obtained by a one-step optimization of seed dilution and protein concentration using a two-dimensional grid screen. The crystals belonged to the primitive tetragonal space groupP43212, with unit-cell parametersa = b = 61.55,c= 222.81 Å. Complete data sets were collected from native and selenomethionine-substituted protein crystals at 100 K to 2.6 and 2.0 Å resolution, respectively.

scholarly journals Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1

2015 ◽  
Vol 71 (3) ◽  
pp. 261-265 ◽  
Author(s):  
Seoung Min Bong ◽  
Seung Won Yang ◽  
Ji-Woong Choi ◽  
Seung Jun Kim ◽  
Byung Il Lee
Keyword(s):  
Escherichia Coli ◽  
Polyethylene Glycol ◽  
Synchrotron Radiation ◽  
Crystallographic Analysis ◽  
Asymmetric Unit ◽  
Related Protein ◽  
Unit Cell Parameters ◽  
Solvent Content ◽  
X Ray ◽  
Cell Parameters

Myotubularin-related protein 1 is a phosphatase that dephosphorylates phospholipids such as phosphatidylinositol 3-phosphate or phosphatidylinositol 3,5-bisphosphate. In this study, human MTMR1 was overexpressed inEscherichia coli, purified and crystallized at 277 K using polyethylene glycol 20 000 as a precipitant. Diffraction data were collected to 2.0 Å resolution using synchrotron radiation. The crystals belonged to space groupP1, with unit-cell parametersa= 67.219,b= 96.587,c= 97.581 Å, α = 87.597, β = 86.072, γ = 77.327°. Assuming the presence of four molecules in the asymmetric unit, the calculated Matthews coefficient value was 2.61 Å3 Da−1and the corresponding solvent content was 52.9%.

scholarly journals Purification, crystallization and preliminary X-ray data collection of the N-terminal domain of the 26S proteasome regulatory subunit p27 and its complex with the ATPase domain of Rpt5 fromMus musculus

2014 ◽  
Vol 70 (5) ◽  
pp. 611-615
Author(s):  
Wentao Diao ◽  
Xue Yang ◽  
Hao Zhou
Keyword(s):  
Unit Cell ◽  
26S Proteasome ◽  
Regulatory Subunit ◽  
Atpase Domain ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Solvent Content ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

The protein 26S proteasome regulatory subunit p27 is one of the four chaperones that help in the assembly of the 19S regulatory particle (RP) of the 26S proteasome. In the present work, the N-terminus of p27 (residues 1–128) fromMus musculuswas cloned, expressed, purified and crystallized alone and in complex with the C-terminal ATPase domain of Rpt5 (residues 173–442). The crystals of p27(1–128)diffracted to 1.7 Å resolution and belonged to space groupP212121, with unit-cell parametersa= 26.79,b= 30.39,c= 145.06 Å. Resolution-dependent Matthews coefficient probability analysis suggested the presence of only one molecule per asymmetric unit, with 40.5% solvent content and aVMvalue of 2.02 Å3 Da−1. The crystal of the p27(1–128)–Rpt5(173–442)complex diffracted to 4 Å resolution and belonged to space groupP222, with unit-cell parametersa= 75.93,b= 76.08,c= 336.85 Å. The presence of four heterodimers in the asymmetric unit with 53.2% solvent content and aVMvalue of 2.63 Å3 Da−1or five heterodimers in the asymmetric unit with 41.5% solvent content and aVMvalue of 2.10 Å3 Da−1is assumed.

scholarly journals Expression, purification, crystallization and preliminary X-ray analysis of glucose-1-phosphate uridylyltransferase (GalU) fromErwinia amylovora

2014 ◽  
Vol 70 (9) ◽  
pp. 1249-1251 ◽  
Author(s):  
Mirco Toccafondi ◽  
Michele Cianci ◽  
Stefano Benini
Keyword(s):  
Erwinia Amylovora ◽  
Search Model ◽  
Data Sets ◽  
Molecular Replacement ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
E Coli ◽  
Maximum Resolution ◽  
His Tag

Glucose-1-phosphate uridylyltransferase fromErwinia amylovoraCFPB1430 was expressed as a His-tag fusion protein inEscherichia coli. After tag removal, the purified protein was crystallized from 100 mMTris pH 8.5, 2 Mammonium sulfate, 5% ethylene glycol. Diffraction data sets were collected to a maximum resolution of 2.46 Å using synchrotron radiation. The crystals belonged to the hexagonal space groupP62, with unit-cell parametersa= 80.67,b= 80.67,c = 169.18. The structure was solved by molecular replacement using the structure of theE. colienzyme as a search model.

scholarly journals Expression, purification, crystallization and preliminary X-ray analysis of the human NORE1 SARAH domain

2012 ◽  
Vol 68 (7) ◽  
pp. 813-815 ◽  
Author(s):  
Hye Jin Kim ◽  
Eunha Hwang ◽  
Young-Hyun Han ◽  
Saehae Choi ◽  
Woo Cheol Lee ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Kinase ◽  
Unit Cell ◽  
Diffusion Method ◽  
Hanging Drop ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Apoptotic Protein ◽  
Vapour Diffusion

NORE1 is an important tumour suppressor in human cancers that interacts with the pro-apoptotic protein kinase MST1/2 through SARAH domains. The SARAH domain (residues 366–413) of human NORE1 was expressed inEscherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystal diffracted to 2.7 Å resolution and belonged to space groupP6122, with unit-cell parametersa=b= 73.041,c = 66.092 Å, α = β = 90, γ = 120°.

Crystallization and preliminary X-ray analysis of a complex between the Bowman–Birk trypsin inhibitor from barley and porcine pancreatic trypsin

1999 ◽  
Vol 55 (6) ◽  
pp. 1244-1246 ◽  
Author(s):  
Young Sil Kim ◽  
Hyun Kyu Song ◽  
Se Won Suh
Keyword(s):  
Polyethylene Glycol ◽  
Trypsin Inhibitor ◽  
Unit Cell ◽  
X Rays ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Orthorhombic Space Group ◽  
Solvent Content ◽  
X Ray ◽  
Cell Parameters

A 1:2 complex between the Bowman–Birk trypsin inhibitor from barley seeds and porcine pancreatic trypsin has been crystallized at 291 K using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.10, b = 88.38 and c = 203.65 Å. The asymmetric unit contains two monomers of the complex, with a corresponding Vm of 2.41 Å3 Da−1 and a solvent content of 49%. Native data to 2.2 Å resolution have been collected at 100 K using synchrotron X-rays.

Crystallization and preliminary crystallographic studies of ribosome recycling factor from Escherichia coli

2000 ◽  
Vol 56 (1) ◽  
pp. 84-85 ◽  
Author(s):  
Jungmin Yun ◽  
Wookhyun Kim ◽  
Sung Chul Ha ◽  
Soo-Hyun Eom ◽  
Se Won Suh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Final Stage ◽  
Unit Cell ◽  
Ribosome Recycling Factor ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Peg 400

Ribosome recycling factor (RRF) catalyzes the disassembly of a termination complex during the final stage of protein synthesis. RRF from Escherichia coli has been crystallized with PEG 400 as precipitant at 287 K. The crystal belongs to the trigonal space group P3121 (or P3221), with unit-cell parameters a = b = 48.08, c = 141.67 Å. Native data were collected from a frozen crystal to a resolution of 3.0 Å on a Cu Kα rotating-anode X-ray source.

Crystallization and preliminary X-ray studies of metallothionein II from rabbit liver

1999 ◽  
Vol 55 (6) ◽  
pp. 1242-1243 ◽  
Author(s):  
Yu An ◽  
Genpei Li ◽  
Binggen Ru
Keyword(s):  
Sodium Citrate ◽  
Unit Cell ◽  
Rabbit Liver ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Citrate Buffer ◽  
Solvent Content ◽  
X Ray ◽  
Cell Parameters ◽  
Sodium Citrate Buffer

Metallothionein II (Mw = 6.8 kDa), induced by cadmium and purified from rabbit liver, has been crystallized in space group P6222 or P6422. The unit-cell parameters were a = b = 113.4, c = 219.1 Å, α = β = 90.0, γ = 120.0° when crystallized from sodium citrate buffer and a = b = 113.4, c = 219.6 Å, α = β = 90.0, γ = 120.0° when crystallized from Tris–HCl buffer. There are 12 molecules per asymmetric unit and the solvent content is about 57%.

scholarly journals Crystal Structure Refinements of Four Monazite Samples from Different Localities

Minerals ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1028 ◽  
Author(s):  
M. Mashrur Zaman ◽  
Sytle M. Antao
Keyword(s):  
Crystal Structure ◽  
Electron Probe ◽  
Unit Cell Volume ◽  
Unit Cell ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Large Unit Cell ◽  
A Site

This study investigates the crystal chemistry of monazite (APO4, where A = Lanthanides = Ln, as well as Y, Th, U, Ca, and Pb) based on four samples from different localities using single-crystal X-ray diffraction and electron-probe microanalysis. The crystal structure of all four samples are well refined, as indicated by their refinement statistics. Relatively large unit-cell parameters (a = 6.7640(5), b = 6.9850(4), c = 6.4500(3) Å, β = 103.584(2)°, and V = 296.22(3) Å3) are obtained for a detrital monazite-Ce from Cox’s Bazar, Bangladesh. Sm-rich monazite from Gunnison County, Colorado, USA, has smaller unit-cell parameters (a = 6.7010(4), b = 6.9080(4), c = 6.4300(4) Å, β = 103.817(3)°, and V = 289.04(3) Å3). The a, b, and c unit-cell parameters vary linearly with the unit-cell volume, V. The change in the a parameter is large (0.2 Å) and is related to the type of cations occupying the A site. The average <A-O> distances vary linearly with V, whereas the average <P-O> distances are nearly constant because the PO4 group is a rigid tetrahedron.

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